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Literature DB >> 22132051

Creating novel protein scripts beyond natural alphabets.

Abstract

Natural proteins are concatenated amino acids with definite handedness or chirality, with their spatial orientation being preferentially left handed or L-chiral. This paper discusses the biophysics of stereo-chemical perturbation to proteins using D-(α) amino acid and its utility as an additional design alphabet while scripting novel protein structures.

Entities: Chemical

Keywords: Heterochiral proteins; Polypeptide stereochemistry; Protein design; Protein structure energetics

Year: 2011 PMID： 22132051 PMCID： PMC3065589 DOI： 10.1007/s11693-011-9068-5

Source DB: PubMed Journal: Syst Synth Biol ISSN： 1872-5325

59 in total

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Journal: Proc Natl Acad Sci U S A Date: 2004-08-16 Impact factor: 11.205

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Journal: Chem Commun (Camb) Date: 2004-09-20 Impact factor: 6.222

5. Role of backbone solvation in determining thermodynamic beta propensities of the amino acids.

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Journal: Proc Natl Acad Sci U S A Date: 2002-01-22 Impact factor: 11.205

6. Homochiral stereochemistry: the missing link of structure to energetics in protein folding.

Authors: Anil Kumar; Vibin Ramakrishnan; Ranjit Ranbhor; Kirti Patel; Susheel Durani
Journal: J Phys Chem B Date: 2009-12-24 Impact factor: 2.991

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Journal: Science Date: 1988-06-17 Impact factor: 47.728

9. A novel main-chain anion-binding site in proteins: the nest. A particular combination of phi,psi values in successive residues gives rise to anion-binding sites that occur commonly and are found often at functionally important regions.